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Literature summary for 1.13.11.33 extracted from

  • Walther, M.; Wiesner, R.; Kuhn, H.
    Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium (2004), J. Biol. Chem., 279, 3717-3725.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
F412E mutation slightly impairs membrane binding, mutant enzyme shows 29% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
F70H mutation impairs membrane binding, mutant enzyme shows 53% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
L195E mutation impairs membrane binding, mutant enzyme shows 42% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
L71K mutation impairs membrane binding, mutant enzyme shows 50% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
W181E mutation strongly impairs membrane binding, mutant enzyme shows 34% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
Y15E mutation impairs membrane binding, mutant enzyme shows 61% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
Y292E mutation slightly impairs membrane binding, mutant enzyme shows 112% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme associates to biomembranes primarily via hydrophobic interactions between surface-exposed apolar amino acid side chains and membrane lipids. Calcium supports membrane binding probably by forming salt bridges between the negatively charged head groups of membrane phospholipids and acidic surface amino acids of the membrane Oryctolagus cuniculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ at 0.005-0.05 mM is required for efficient membrane binding Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonic acid + O2
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Oryctolagus cuniculus (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid + (12S,5Z,8Z,10E,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid the ratio of (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid to (12S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid is 20 for the wild-type enzyme ?

Synonyms

Synonyms Comment Organism
15-LOX
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Oryctolagus cuniculus